Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete

Abstract

A novel extracellular phospholipase C (PLC) was purified from a marine streptomycete. It had a molecular mass of 28 kDa as estimated by SDS-polyacrylamide gel electrophoresis. Its enzyme activity was optimal at pH 8.0 at 45 °C. The PLC hydrolyzed only phosphatidylcholine. Its activity was enhanced 300% by Na+ (200 mM), suggesting that the purified PLC is a typical marine-type enzyme.